Bounds on higher-order Lorentz-violating photon sector coefficients from an asymmetric optical ring resonator experiment

Optical resonators provide a powerful tool for testing aspects of Lorentz invariance. Here, we present a reanalysis of an experiment where a path asymmetry was created in an optical ring resonator by introducing a dielectric prism in one arm. The frequency difference of the two fundamental counter-propagating modes was then recorded as the apparatus was orientation-modulated in the laboratory. By assuming that the minimal Standard-Model Extension coefficients vanish we are able to place bounds on higher-order parity-odd Lorentz-violating coefficients of the Standard-Model Extension. The results presented in this work set the first constraints on two previously unbounded linear combinations of d=8 parity-odd nonbirefringent nondispersive coefficients of the photon sector.Comment: 6 pages, 4 figures, 3 tables, accepted for publication in Physics Letters

Knickpoints in Martian channels indicate past ocean levels

On Mars, the presence of extensive networks of sinuous valleys and large channels provides evidence for a wetter and warmer environment where liquid water was more abundant than it is at present. We undertook an analysis of all major channel systems on Mars and detected sharp changes in elevation along the river long profiles associated with steep headwall theatre-like valleys and terraces left downstream by channel incision. These breaks in channel longitudinal slope, headwalls and terraces exhibit a striking resemblance with terrestrial fluvial features, commonly termed 'knickpoints'. On Earth, such knickpoints can be formed by more resistant bedrock or where changes in channel base-level have initiated erosion that migrates upstream (such as tectonic uplift or sea level change). We observed common elevations of Martian knickpoints in eleven separate channel systems draining into the Martian Northern lowlands. Numerical modeling showed that the common elevations of some of these knickpoints were not random. As the knickpoints are spread across the planet, we suggest that these Martian knickpoints were formed in response to a common base level or ocean level rather than local lithology. Thus, they potentially represent a record of past ocean levels and channel activity on Mars

Nonenzymatically Glucosylated Albumin: In Vitro Preparation and Isolation from Normal Human Serum

Incubation of human serum with D-[6-3H]glucose resulted in the gradual accumulation of radioactivity in acid-precipitable material. Upon chromatography on Sephadex G-200, radioactivity was found associated with each of the major molecular weight classes of serum protein. Purified human serum albumin was also glucosylated in vitro upon exposure to D-[6-3H]glucose in phosphate-buffered saline. The glucosylated and unmodified albumins were separated by ion exchange chromatography. The physiological significance of these observations in vitro was confirmed by the isolation and quantitation of glucosylated albumin from normal human serum. Glucosylated albumin represents approximately 6 to 15% of total serum albumin in normal adults. The post-translational modification appears to occur by a nonenzymatic process analogous to that responsible for glucosylation of hemoglobin A to hemoglobin AIc, i.e. through Schiff base formation and Amadori rearrangement to a ketoamine derivative

Inulin-\u3csup\u3e125\u3c/sup\u3eI-Tyramine, an Improved Residualizing Label for Studies on Sites of Catabolism of Circulating Proteins

Residualizing labels for protein, such as dilactitol-125I-tyramine (125I-DLT) and cellobiitol-125I-tyramine, have been used to identify the tissue and cellular sites of catabolism of long-lived plasma proteins, such as albumin, immunoglobulins, and lipoproteins. The radioactive degradation products formed from labeled proteins are relatively large, hydrophilic, resistant to lysosomal hydrolases, and accumulate in lysosomes in the cells involved in degradation of the carrier protein. However, the gradual loss of the catabolites from cells (t1/2 approximately 2 days) has limited the usefulness of residualizing labels in studies on longer lived proteins. We describe here a higher molecular weight (Mr approximately 5000), more efficient residualizing glycoconjugate label, inulin-125I-tyramine (125I-InTn). Attachment of 125I-InTn had no effect on the plasma half-life or tissue sites of catabolism of asialofetuin, fetuin, or rat serum albumin in the rat. The half-life for hepatic retention of degradation products from 125I-InTn-labeled asialofetuin was 5 days, compared to 2.3 days for 125I-DLT-labeled asialofetuin. The whole body half-lives for radioactivity from 125I-InTn-, 125I-DLT-, and 125I-labeled rat serum albumin were 7.5, 4.3, and 2.2 days, respectively. The tissue distribution of degradation products from 125I-InTn-labeled proteins agreed with results of previous studies using 125I-DLT, except that a greater fraction of total degradation products was recovered in tissues. Kinetic analyses indicated that the average half-life for retention of 125I-InTn degradation products in tissues is approximately 5 days and suggested that in vivo there are both slow and rapid routes for release of degradation products from cells. Overall, these experiments indicate that 125I-InTn should provide greater sensitivity and more accurate quantitative information on the sites of catabolism of long-lived circulating proteins in vivo

Extreme Flood Sediment Production and Export Controlled by Reach‐Scale Morphology

Rapid earth surface evolution is discrete in nature, with short-duration extreme events having a widespread impact on landscapes despite occurring relatively infrequently. Here, we exploit a unique opportunity to identify the broad, process-based, controls on sediment production and export during extreme rainfall-runoff events through a multi-catchment analysis. A 3 hr extreme rainfall event generated significantly different impacts across three catchments, ranging from (a) sediment export exceeding two orders of magnitude more than the typical long term average to (b) a minimal impact, with this variability primarily controlled by catchment steepness and the presence of reach-scale morphological transitions caused by postglacial landscape adjustment. In any catchment worldwide where populations are at risk, we highlight the importance of combining topographic analysis with detailed mapping of channel bed material (e.g., presence of transitions between process domains) and identification of sediment sources within morphological transition zones for accurately predicting the impact of extreme events

Glycation of Amino Groups in Protein

Ribonuclease A has been used as a model protein for studying the specificity of glycation of amino groups in protein under physiological conditions (phosphate buffer, pH 7.4, 37 “C). Incubation of RNase with glucose led to an enhanced rate of inactivation of the enzyme relative to the rate of modification of lysine residues, suggesting preferential modification of active site lysine residues. Sites of glycation of RNase were identified by amino acid analysis of tryptic peptides isolated by reverse-phase high pressure liquid chromatography and phenylboronate affinity chromatography. Schiff base adducts were trapped with Na- BH&N and the a-amino group of Lys-1 was identified as the primary site (80-90%) of initial Schiff base formation on RNase. In contrast, Lys-41 and Lys-7 in the active sitaec counted for about 38 and 29%, respectively, of ketoamine adducts formed via the Amadori rearrangement. Other sites reactive in ketoamine formation included Ne-Lys-1 (15%), N-Lys-1 (9%), and Lys-37 (9%w) hich are adjacent to acidic amino acids. The remaining six lysine residues in RNase, which are located on the surface of the protein, were relatively inactive in forming either the Schiff base or Amadori adduct. Both the equilibrium Schiff base concentration and the rate of the Amadori rearrangement at each site were found to be important in determining the specificity of glycation of RNase

Identification of N epsilon-Carboxymethyllysine as a Degradation Product of Fructoselysine in Glycated Protein

The chemistry of Maillard or browning reactionosf glycated proteins was studied using the model compound, Nu-formyl-W-fructoselysine(f FL), an analog of glycated lysine residues in protein. Incubation of fFL (15 mM) at physiological pH and temperature in 0.2 M phosphate buffer resulted in formation of lVcarboxymethyllysine (CML) in about 40% yield after 15 days. CML was formed by oxidative cleavage of fFL between C-2 and C-3 of the carbohydrate chain and erythronic acid (EA) was identified a s , the split product formed in the reaction. Neither CML nor EA was formed from fFL under a nitrogen atmosphere. The rate of formation of CML was dependent on phosphate concentration in the incubation mixture and the reaction was shown to occur by a free radical mechanism. CML was also identified by amino acid analysis in hydrolysates of both poly-L-lysine and bovine pancreatic ribonuclease glycated in phosphate buffer under air. CML was also detected in human lens proteins and tissue collagens by HPLC and the identification was confirmed by gas chromatography/mass spectroscopy. The presence of both CML and EA in human urine suggests that they are formed by degradation of glycated proteins in vivo. The browning of fFL incubation mixtures proceeded to a greater extent under a nitrogen versus an air atmosphere, suggesting that oxidative degradation of Amadori adducts to form CML may limit the browning reactions of glycated proteins. Since the reaction products, CML and EA, are relatively inert, both chemically and metabolically, oxidative cleavage of Amadori adducts may have a role in limiting the consequences of protein glycation in the body

Rôle d'un intermédiaire lipidique dans le transfert du mannose à des accepteurs glycoprotéiques endogènes chez Aspergillus niger

AbstractPrevious studies from this laboratory have shown that a particulate preparation from Aspergillus niger catalyses the incorporation of mannose, from GDP-mannose, into a lipid fraction which has been identified as polyprenyl phosphate mannose (PPM). The results of kinetic studies presented in this communication suggest that PPM serves as an intermediate in the ensymatic transfer of mannosyl unit from GDP-mannose to endogenous glycoproteins. β-elimination or Pronase treatment and subsequent dialysis result respectively in 70% or 90% release of radioactivity. The absence of passive penetration of GDP-mannose across microsome membranes and the inhibitory effect of palmityl-CoA on mannose transfer are in good agreement with the involvement of PPM in the transport of mannose across membranes

Role of the Maillard Reaction in Aging of Tissue Proteins: Advanced Glycation End Product-Dependent Increase in Imidazolium Cross-Links in Human Lens Proteins

Dicarbonyl compounds such as glyoxal and methylglyoxal are reactive dicarbonyl intermediates in the nonenzymatic browning and cross-linking of proteins during the Maillard reaction. We describe here the quantification of glyoxal and methylglyoxal-derived imidazolium cross-links in tissue proteins. The imidazolium salt cross-links, glyoxal-lysine dimer (GOLD) and methylglyoxal-lysine dimer (MOLD), were measured by liquid chromatography/mass spectrometry and were present in lens protein at concentrations of 0. 02-0.2 and 0.1-0.8 mmol/mol of lysine, respectively. The lens concentrations of GOLD and MOLD correlated significantly with one another and also increased with lens age. GOLD and MOLD were present at significantly higher concentrations than the fluorescent cross-links pentosidine and dityrosine, identifying them as major Maillard reaction cross-links in lens proteins. Like the N-carboxy-alkyllysines Nepsilon-(carboxymethyl)lysine and Nepsilon-(carboxyethyl)lysine, these cross-links were also detected at lower concentrations in human skin collagen and increased with age in collagen. The presence of GOLD and MOLD in tissue proteins implicates methylglyoxal and glyoxal, either free or protein-bound, as important precursors of protein cross-links formed during Maillard reactions in vivo during aging and in disease

[\u3csup\u3e3\u3c/sup\u3eH]‑Raffinose, a Novel Radioactive Label for Determining Organ Sites of Catabolism of Proteins in the Circulation

The primary tissue sites of catabolism of plasma proteins with long circulating half-lives are unknown. It has been difficult to identify these sites because plasma proteins are delivered to tissues at relatively slow rates but are rapidly degraded intracellularly within lysosomes. Therefore, a tracer attached to protein is lost from the site of uptake before an amount sufficient for quantitation can accumulate. We hypothesized that sucrose (Glupal-2 /3Fruf) would be a useful label to circumvent this difficulty because of the stability of sucrose in lysosomes; and thus, sucrose should remain in tissue long after the protein to which it was attached had been degraded to products released from the lysosome. [G-3HJRaffinose (RAF, Galpal- Glupcwl- 2flFruf) was selected as the vehicle for attaching sucrose to protein. [31XjRAF was converted to the C-6 aldehydogalactose form with galactose oxidase and then covalently coupled to protein by reductive amination using NaBH3CN. [‘H]RAF was coupled first to two relatively long lived plasma proteins, bovine serum albumin and fetuin. The half-lives of these proteins in the rat circulation (&,* = -24 h) was unchanged, suggesting that RAF did not alter the normal mechanisms of protein clearance. When attached to short lived proteins with known sites of catabolism, such as asialofetuin, RNase B, and heatdenatured albumin, neither the tissue nor cellular sites of uptake of the proteins were altered. Thus, 13H]RAFasialofetuin was recovered almost exclusively (\u3e90%) in the liver parenchymal cell fraction, while both [JHJRAF-labeled RNase B and heat-denatured albumin were recovered primarily (\u3e85%) in nonparenchymal cells. In addition, the RAF label was observed to reside stably (tl,2 \u3e 100 h) in the liver following degradation of the carrier protein; in contrast, radioactivity from “‘Ilabeled asialofetuin or RNase B was rapidly (tl,z \u3c 30 min) lost from liver. Radioactivity from 13H]RAF-proteins was recovered in a lysosomally enriched subcellular fraction in liver and consisted of a low molecular weight species (-llOO), containing both glucose and fructose in a ratio similar to that in the original protein. The results of these studies establish that 13H]RAF useful radioactive tracer for detecting the tissue and cellular sites of catabolism of long lived circulating proteins